Production of xylo-oligosaccharides by immobilized-stabilized derivatives of endo-xylanase from Streptomyces halstedii

Aragon, Caio Casale; Mateo, César; Ruiz‐Matute, Ana I.; Corzo, Nieves; Fernández‐Lorente, Gloria; Sevillano, Laura; Díaz, Margarita; Santamaría, Ramón I.; Guisán, José M.

doi:10.1016/j.procbio.2013.01.010

Cited by 31 publications

(29 citation statements)

References 23 publications

(1 reference statement)

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“…This is due to adsorption on support increases the stability or conformational rigidity of enzyme. A similar increase in optimum temperature range has been reported for endoxylanase immobilized on agarose‐glyoxal and chitosan‐glutaraldehyde and Nickel‐chelate Eupergit C, entrapped in chitosan chitin and PEG Net‐Cloth, adsorbed on Aluminum hydroxide particles, covalently bound to glyoxyl‐agarose and cyanuric chloride activated magnetic nanoparticles, bifunctional xylanase (ATXX) immobilized on carbon‐coated chitosan nanoparticles and xylanase immobilized on mesoporous silica coated chitosan . The increase in optimal temperature for activity of xylanase is independent of type of immobilization as both non‐covalent adsorption and covalent immobilization resulted in increase of optimal temperature.…”

Section: Resultssupporting

confidence: 69%

“…Among these three types of materials, CMK‐3 retained more initial activity since XynC and CMK‐3 interaction is mostly hydrophobic compared to SBA‐15 and ZMF‐127 which are more likely electro statistics . Endoxylanase (XynA) from B. subtilis immobilized on agarose activated with glyoxal groups and endoxylanase from S. halstedii immobilized on glyoxyl‐agarose have been reported to retain initial activity for 10 cycles. Xylanase from P. occitanis Pol6 immobilized on Nickel‐chelate Eupergit C has been reported to retain 50% ofinitial activity after 5 cycles .…”

Section: Resultsmentioning

confidence: 99%

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Immobilization of Recombinant Endo‐1,4‐β‐xylanase on Ordered Mesoporous Matrices for Xylooligosaccharides Production

et al. 2019

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Xylooligosaccharides (XOS) are emerging prebiotics, widely used in food, medicine and health care. XOS are produced by hydrolysis of xylan by acid or endoxylanase enzyme. Xylanase hydrolysis is preferred over acid due to its high specificity and absence of formation of non‐toxic byproducts. Immobilized xylanase improves enzyme‐stability and efficacy of XOS production through its repeated use. Though there are a few xylanases immobilized on conventional organic polymers for XOS production, immobilization of xylanse on mesoporous inorganic materials have not been investigated for XOS production. In this study, the recombinant endo‐1, 4‐β‐D‐xylanase (XynC) of B.subtilis KCX006 was purified and immobilized on ordered mesoporous matrices of carbon (CMK‐3), silica (SBA‐15) and zirconia (ZMF‐127). The immobilized‐XynC was characterized and used for XOS production by recycling. The recovered activity (RA) of immobilized‐XynC varied between 55 to 84%. The maximum RA was observed for XynC immobilized on ZMF‐127 matrix. All immobilized‐XynC had optimum pH similar to that of free‐XynC. But all immobilized‐XynC gained broader temperature range (50‐65°C) for optimal catalytic activity when compared with the free‐XynC. Immobilization of XynC resulted in higher Km due to substrate diffusion limit. All immobilized‐XynC produced free‐XOS of DP 2–6 (X2‐X6) and substituted‐XOS from beechwood xylan and extracted crude xylans from sorghum stalks and sugarcane bagasse (SCB). The XynC immobilized on SBA‐15 produced higher proportions of X2‐X6 compared to ZMF‐127 and CMK‐3. The XynC immobilized on SBA‐15 and CMK‐3 retained higher activity of 85–93% after four batches of repeated use. The observed efficiency of XynC immobilized on CMK‐3 and SBA‐15 are higher than the reported values. The results showed that XynC immobilized on mesoporous carbon and silica matrices would be useful for production of XOS by enzyme recycling.

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Section: Resultssupporting

confidence: 69%

Section: Resultsmentioning

confidence: 99%

Immobilization of Recombinant Endo‐1,4‐β‐xylanase on Ordered Mesoporous Matrices for Xylooligosaccharides Production

et al. 2019

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“…High temperatures lead to higher reaction velocities and, consequently, lower reactor volume. Besides, they may be useful to increase xylan solubility and to prevent microbial contamination [47]. The three derivatives of XynA obtained here were tested for their thermal stability and compared with the free enzyme.…”

Section: Xyna Thermal Stabilitymentioning

confidence: 99%

“…This result was unexpected, in view of the low number of lysines on the XynA surface. The formation of several bonds between enzyme and the support is necessary to increase the thermal stability of enzymes, and particularly for xylanase [7,30,47,48], but XynA has only three lysines in the same plane. Consequently, this is the maximum number of attachments that may be achieved.…”

Section: Xyna Thermal Stabilitymentioning

confidence: 99%

Immobilization and stabilization of an endoxylanase from Bacillus subtilis (XynA) for xylooligosaccharides (XOs) production

et al. 2016

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a b s t r a c tXylooligosaccharides (XOs) are small oligomers constituted by 2−10 units of xylan monomers, with important nutraceutical properties. They can be produced through hydrolysis of xylan catalyzed by an endoxylanase. The use of immobilized and stabilized enzymes may decrease the industrial process costs. In this study, XynA, a recombinant enzyme from B. subtilis, was immobilized in three different supports: agarose and chitosan activated with glyoxal groups and chitosan activated with glutaraldehyde. High immobilization yields were obtained, 100% for agarose-glyoxal and chitosan-glutaraldehyde, 82% for chitosan-glyoxal, with recovered activities of 42.7 (±1.3), 10.7 ± 0.8 and 53.6% (± 1.7), respectively. A great increase in the thermal stability of the enzyme (at 56 • C, pH 5.5) was achieved for the glyoxal derivatives: 75-fold for chitosan and 8600-fold for agarose. The great thermal stability obtained to the derivative agarose-glyoxal can be explained by the enzyme immobilization through lysine residues located in unstable sites of the protein structure. The agarose-glyoxal derivative was tested in the production of XOs (X2, X3 and X4) from soluble and conventional birchwood xylan, reaching approximately 20% of conversion in 3 h and 23% in 24 h, without the undesirable xylose production. After 10 cycles of hydrolysis, the conversion remained almost unchanged.

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“…Endo-␤-1, 4-xylanase (EC 3.2.1.8, further referred to as xylanase) is one of the important enzymes involved in the degradation of xylan, which is the most abundant natural cell wall polysaccharide after cellulose [1][2][3]. In past 20 years, xylanase has drawn considerable research interest mainly because of its known and potential application, such as production of xylooligosaccharides (XOs) in the food industry and conversion of agricultural by-product into reducing sugar [4][5][6][7]. These applications need enzymes to retain high activity after being used several times at drastic process conditions (high temperature, high ion concentration, acidic, or alkaline environment) and to easily recover from reaction mixtures for reuse.…”

Section: Introductionmentioning

confidence: 99%

An immobilized bifunctional xylanase on carbon-coated chitosan nanoparticles with a potential application in xylan-rich biomass bioconversion

Liu

Huo

Jin

2015

Journal of Molecular Catalysis B: Enzymatic

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Production of xylo-oligosaccharides by immobilized-stabilized derivatives of endo-xylanase from Streptomyces halstedii

Cited by 31 publications

References 23 publications

Immobilization of Recombinant Endo‐1,4‐β‐xylanase on Ordered Mesoporous Matrices for Xylooligosaccharides Production

Immobilization of Recombinant Endo‐1,4‐β‐xylanase on Ordered Mesoporous Matrices for Xylooligosaccharides Production

Immobilization and stabilization of an endoxylanase from Bacillus subtilis (XynA) for xylooligosaccharides (XOs) production

An immobilized bifunctional xylanase on carbon-coated chitosan nanoparticles with a potential application in xylan-rich biomass bioconversion

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